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Volumn 579, Issue 16, 2005, Pages 3369-3375

A genome-wide analysis of sumoylation-related biological processes and functions in human nucleus

Author keywords

Perception of sound; Signal transduction; SUMO; Sumoylation; Transcription factor

Indexed keywords

PROTEOME; SUMO PROTEIN; TRANSCRIPTION FACTOR;

EID: 20444375092     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.04.076     Document Type: Article
Times cited : (46)

References (37)
  • 1
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • G. Gill SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev. 18 2004 2046 2059
    • (2004) Genes Dev. , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 4
  • 6
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO. a role in transcriptional regulation
    • A. Verger, J. Perdomo, and M. Crossley Modification with SUMO. A role in transcriptional regulation EMBO Rep. 4 2003 137 142
    • (2003) EMBO Rep. , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 7
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: New partners in transcriptional regulation
    • D. Schmidt, and S. Muller PIAS/SUMO: new partners in transcriptional regulation Cell. Mol. Life Sci. 60 2003 2561 2574
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2561-2574
    • Schmidt, D.1    Muller, S.2
  • 8
    • 0037382641 scopus 로고    scopus 로고
    • Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity
    • G. Gill Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity Curr. Opin. Genet. Dev. 13 2003 108 113
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 108-113
    • Gill, G.1
  • 9
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress
    • T.T. Huang, S.M. Wuerzberger-Davis, Z.H. Wu, and S. Miyamoto Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress Cell 115 2003 565 576
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 10
    • 0036069554 scopus 로고    scopus 로고
    • Top-SUMO wrestles centromeric cohesion
    • B.A. Pinsky, and S. Biggins Top-SUMO wrestles centromeric cohesion Dev. Cell 3 2002 4 6
    • (2002) Dev. Cell , vol.3 , pp. 4-6
    • Pinsky, B.A.1    Biggins, S.2
  • 12
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • D.C. Schwartz, and M. Hochstrasser A superfamily of protein tags: ubiquitin, SUMO and related modifiers Trends Biochem. Sci. 28 2003 321 328
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 13
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • H. Saitoh, and J. Hinchey Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3 J. Biol. Chem. 275 2000 6252 6258
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 14
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus
    • K.M. Bohren, V. Nadkarni, J.H. Song, K.H. Gabbay, and D. Owerbach A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus J. Biol. Chem. 279 2004 27233 27238
    • (2004) J. Biol. Chem. , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 15
    • 4744360999 scopus 로고    scopus 로고
    • A proteome-wide approach identifies sumoylated substrate proteins in yeast
    • V.G. Panse, U. Hardeland, T. Werner, B. Kuster, and E. Hurt A proteome-wide approach identifies sumoylated substrate proteins in yeast J. Biol. Chem. 279 2004 41346 41351
    • (2004) J. Biol. Chem. , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.5
  • 16
    • 14644392172 scopus 로고    scopus 로고
    • Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome
    • D.D. Wykoff, and E.K. O'Shea Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome Mol. Cell. Proteomics 4 2005 73 83
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 73-83
    • Wykoff, D.D.1    O'Shea, E.K.2
  • 19
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
    • W. Zhou, J.J. Ryan, and H. Zhou Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses J. Biol. Chem. 279 2004 32262 32268
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 20
    • 8544273758 scopus 로고    scopus 로고
    • Global analysis of protein sumoylation in Saccharomyces cerevisiae
    • J.A. Wohlschlegel, E.S. Johnson, S.I. Reed, and J.R. Yates III Global analysis of protein sumoylation in Saccharomyces cerevisiae J. Biol. Chem. 279 2004 45662 45668
    • (2004) J. Biol. Chem. , vol.279 , pp. 45662-45668
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates III, J.R.4
  • 22
    • 14244249406 scopus 로고    scopus 로고
    • Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates
    • C.B. Gocke, H. Yu, and J. Kang Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates J. Biol. Chem. 280 2005 5004 5012
    • (2005) J. Biol. Chem. , vol.280 , pp. 5004-5012
    • Gocke, C.B.1    Yu, H.2    Kang, J.3
  • 23
    • 2442703973 scopus 로고    scopus 로고
    • Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins
    • Y. Zhao, S.W. Kwon, A. Anselmo, K. Kaur, and M.A. White Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins J. Biol. Chem. 279 2004 20999 21002
    • (2004) J. Biol. Chem. , vol.279 , pp. 20999-21002
    • Zhao, Y.1    Kwon, S.W.2    Anselmo, A.3    Kaur, K.4    White, M.A.5
  • 27
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • M.S. Rodriguez, C. Dargemont, and R.T. Hay SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting J. Biol. Chem. 276 2001 12654 12659
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 28
    • 1342279419 scopus 로고    scopus 로고
    • SUMO modification of proteins other than transcription factors
    • F.Z. Watts SUMO modification of proteins other than transcription factors Semin. Cell Dev. Biol. 15 2004 211 220
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 211-220
    • Watts, F.Z.1
  • 29
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • E.S. Johnson Protein modification by SUMO Annu. Rev. Biochem. 73 2004 355 382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 30
    • 0035861990 scopus 로고    scopus 로고
    • Automatic clustering of orthologs and in-paralogs from pairwise species comparisons
    • M. Remm, C.E. Storm, and E.L. Sonnhammer Automatic clustering of orthologs and in-paralogs from pairwise species comparisons J. Mol. Biol. 314 2001 1041 1052
    • (2001) J. Mol. Biol. , vol.314 , pp. 1041-1052
    • Remm, M.1    Storm, C.E.2    Sonnhammer, E.L.3
  • 31
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • K. Nakai, and P. Horton PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization Trends Biochem. Sci. 24 1999 34 36
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 33
    • 0346366819 scopus 로고    scopus 로고
    • Widespread production of novel soluble protein isoforms by alternative splicing removal of transmembrane anchoring domains
    • Y. Xing, Q. Xu, and C. Lee Widespread production of novel soluble protein isoforms by alternative splicing removal of transmembrane anchoring domains FEBS Lett. 555 2003 572 578
    • (2003) FEBS Lett. , vol.555 , pp. 572-578
    • Xing, Y.1    Xu, Q.2    Lee, C.3
  • 34
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • N. Blom, T. Sicheritz-Ponten, R. Gupta, S. Gammeltoft, and S. Brunak Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence Proteomics 4 2004 1633 1649
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 35
    • 0034731301 scopus 로고    scopus 로고
    • Identification and characterization of a SUMO-1 conjugation system that modifies neuronal calcium/calmodulin-dependent protein kinase II in Drosophila melanogaster
    • X. Long, and L.C. Griffith Identification and characterization of a SUMO-1 conjugation system that modifies neuronal calcium/calmodulin-dependent protein kinase II in Drosophila melanogaster J. Biol. Chem. 275 2000 40765 40776
    • (2000) J. Biol. Chem. , vol.275 , pp. 40765-40776
    • Long, X.1    Griffith, L.C.2
  • 36
    • 0031831780 scopus 로고    scopus 로고
    • Pleckstrin homology domains: A common fold with diverse functions
    • M.J. Rebecchi, and S. Scarlata Pleckstrin homology domains: a common fold with diverse functions Annu. Rev. Biophys. Biomol. Struct. 27 1998 503 528
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 503-528
    • Rebecchi, M.J.1    Scarlata, S.2
  • 37
    • 2942525287 scopus 로고    scopus 로고
    • Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis
    • T. Li, E. Evdokimov, R.F. Shen, C.C. Chao, E. Tekle, T. Wang, E.R. Stadtman, D.C. Yang, and P.B. Chock Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis Proc. Natl. Acad. Sci. USA 101 2004 8551 8556
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8551-8556
    • Li, T.1    Evdokimov, E.2    Shen, R.F.3    Chao, C.C.4    Tekle, E.5    Wang, T.6    Stadtman, E.R.7    Yang, D.C.8    Chock, P.B.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.